Violacein cytotoxicity on human blood lymphocytes and effect on phosphatases

dc.creatorBromberg, N
dc.creatorJusto, GZ
dc.creatorHaun, M
dc.creatorDuran, N
dc.creatorFerreira, CV
dc.date2005
dc.dateOCT
dc.date2014-11-18T16:40:50Z
dc.date2015-11-26T16:57:20Z
dc.date2014-11-18T16:40:50Z
dc.date2015-11-26T16:57:20Z
dc.date.accessioned2018-03-28T23:44:52Z
dc.date.available2018-03-28T23:44:52Z
dc.identifierJournal Of Enzyme Inhibition And Medicinal Chemistry. Taylor & Francis Ltd, v. 20, n. 5, n. 449, n. 454, 2005.
dc.identifier1475-6366
dc.identifierWOS:000233401700005
dc.identifier10.1080/14756360500273052
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/72781
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/72781
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/72781
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1277633
dc.descriptionGiven the importance of protein phosphorylation in the context of cellular functions, abnormal protein phosphatase activity has been implicated in several diseases, including cancer. These critical roles of protein phosphatases qualify them as potential targets for the development of medicinal compounds that possess distinct modes of action such as violacein. In this work, studies with this natural indolic pigment at a concentration of 10.0 mu mol L-1 demonstrated a 20% activation of total protein phosphatase extracted from human lymphocytes. Although no alteration was observed on protein tyrosine phosphatase (CD45), 30% of inhibition was achieved in cytoplasmatic protein phosphatase activity after incubation with 10.0 mu mol L-1 violacein. Additionally, 5.0 mu mol L-1 of violacein inhibited by 50% the serum tartrate-resistant acid phosphatase activity. Violacein presented toxic effect on lymphocytes with IC50 values of 3 and 10 mu mol L-1 for protein content and protein phosphatase activity, respectively. These findings suggest an important role for protein phosphatases in the mechanisms controlling proliferation and cell death.
dc.description20
dc.description5
dc.description449
dc.description454
dc.languageen
dc.publisherTaylor & Francis Ltd
dc.publisherAbingdon
dc.publisherInglaterra
dc.relationJournal Of Enzyme Inhibition And Medicinal Chemistry
dc.relationJ. Enzym. Inhib. Med. Chem.
dc.rightsfechado
dc.rightshttp://journalauthors.tandf.co.uk/permissions/reusingOwnWork.asp
dc.sourceWeb of Science
dc.subjectprotein phosphatase
dc.subjecttartrate-resistant acid phosphatase
dc.subjectviolacein
dc.subjectlymphocytes
dc.subjectcytotoxicity
dc.subjectinhibition
dc.subjectProtein-tyrosine-phosphatase
dc.subjectPromyelocytic Leukemia-cells
dc.subjectChromobacterium-violaceum
dc.subjectCroton-cajucara
dc.subjectV79 Cells
dc.subjectApoptosis
dc.subjectDehydrocrotonin
dc.subjectActivation
dc.subjectInhibitors
dc.subjectInduction
dc.titleViolacein cytotoxicity on human blood lymphocytes and effect on phosphatases
dc.typeArtículos de revistas


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